Enzymes are biological macromolecule that acts as catalysts and increase the rate of a chemical reaction. Without enzymes, life, as we know about it, would not exist. Enzymes function by deceasing the activation energy and stabilizing the transition state of a chemical reaction without altering the thermodynamic of reaction (#1 Boyer). At the molecular level, enzymes catalyze these reactions by binding to the substrate or reactants to form an enzyme-substrate complex. The reaction takes place while the substrate is bound to the enzyme and converting the substrate to the new product. The new product is then released from the enzyme substrate complex, and the enzyme is then free to bind with more substrate. E+S → ES → E+P (#1 Boyer). Based on this model, the rate at which the product can be produced depends on the amount of enzyme and substrate that are present during the reaction. According to vernier.com, the velocity of the reaction should increase in direct proportion to the concentration of enzyme. In a case where the concentration of substrate is increased and the enzyme concentration is kept constant, the velocity of the reaction will increase rapidly until half of the enzyme becomes saturated with substrate. At this point, the velocity of the reaction will not increase as rapidly. Eventually, the velocity of the reaction will approach a constant rate even when the substrate concentration is increased (#4 vernier.com).
The purposes of this experiment were observed and analyze the effects of changing mushroom Tyrosinase and L-dopa concentrations on reaction rates, and to figure out what type of inhibitor of the Cinnamic acid that was involved in the experiment. The system involved in this lab was L-dopa as a substrate, enzyme...
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...at the maximum substrate concentration. Km represents the Michaelis-Menten constant. It is the substrate concentration at which the reaction velocity is ½ Vmax. At this concentration, half of the enzyme molecule in solution is bounded to the substrate (#5 chemwiki.ucdavis.edu). The Lineweaver-Burk plot is the graph obtained by taking the reciprocal of the Michaelis-Menten Kinetics equation, which give you a linear line (#5 chemwiki.ucdavis.edu). The linear data is easier to read and easier to calculate Vmax, Km than the sigmoidal curve of Michaelis-Menten plot.
According to the vernier.com, the Cinnamic acid is non- competitive inhibitor (#4 vernier.com). Therefore, we expected to see the decrease in Vmax in both Michaelis-Menten and Lineweaver-Burk plot. We also expected to see the sigmoidal curve on Michaelis-Menten plot and linear line on Lineweaver-Burk Plot.
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